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Issue 4, 2010
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SecB—A chaperone dedicated to protein translocation

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Abstract

SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.

Graphical abstract: SecB—A chaperone dedicated to protein translocation

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Publication details

The article was received on 29 Jul 2009, accepted on 25 Sep 2009 and first published on 19 Oct 2009


Article type: Review Article
DOI: 10.1039/B915435C
Citation: Mol. BioSyst., 2010,6, 620-627
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    SecB—A chaperone dedicated to protein translocation

    P. Bechtluft, N. Nouwen, S. J. Tans and A. J. M. Driessen, Mol. BioSyst., 2010, 6, 620
    DOI: 10.1039/B915435C

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